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Volume 271, Number 27, Issue of July 5, 1996 pp. 16090-16096
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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1,25-Dihydroxyvitamin D₃ Stimulates Expression and Translocation of Protein Kinase C and C via a Nongenomic Mechanism and Rapidly Induces Phosphorylation of a 33-kDa Protein in Acute Promyelocytic NB4 Cells

(Received for publication, February 5, 1996, and in revised form, April 15, 1996)

From the Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph, Ontario N1G 2W1, Canada

1,25-Dihydroxyvitamin D₃ (1,25-(OH)₂D₃) primes NB4 cells for 12-O-tetradecanoylphorbol-13-acetate-induced monocytic differentiation in a dose- and sequence-dependent fashion. Experiments utilizing 1,25-(OH)₂D₃ analogues and kinase/phosphatase inhibitors suggested that tyrosine kinase and serine/threonine phosphorylation cascades, rather than vitamin D₃ receptor-mediated signals, were involved in 1,25-(OH)₂D₃ action. Here we show that NB4 cells express the  and  (but not the , , and ) isoforms of protein kinase C (PKC). Both authentic 1,25-(OH)₂D₃ and the nongenomic analogue 1,25-dihydroxyprevitamin D₃ (HF) increased expression of PKC and PKC. PKC and PKC were translocated to the nucleus of the cell in response to 1,25-(OH)₂D₃ or HF. The effects of HF were attenuated by the nongenomic antagonist 1,25-dihydroxyvitamin D₃, suggesting that changes in PKC expression are mediated by a nongenomic signaling pathway. Consistent with the involvement of serine, threonine, and tyrosine phosphorylation cascades mediating 1,25-(OH)₂D₃ action, enhanced phosphorylation of a variety of cellular proteins at serine and threonine residues and the specific enhanced phosphotyrosyl content of a 33-kDa protein (vdrp33) were observed immediately after 1,25-(OH)₂D₃ addition. We propose that 1,25-(OH)₂D₃ primes NB4 cells for 12-O-tetradecanoylphorbol-13-acetate-induced monocytic differentiation by increasing the expression of specific PKC isoforms and inducing the specific phosphorylation of key protein signaling intermediates.

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